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==Crystal structure of 3-deoxy-d-manno-octulosonate 8-phosphate synthase (KDO8PS) from Neisseria meningitidis== | ==Crystal structure of 3-deoxy-d-manno-octulosonate 8-phosphate synthase (KDO8PS) from Neisseria meningitidis== | ||
<StructureSection load='2qkf' size='340' side='right' caption='[[2qkf]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='2qkf' size='340' side='right' caption='[[2qkf]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kdsA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 Neisseria meningitidis serogroup B])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kdsA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 Neisseria meningitidis serogroup B])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-deoxy-8-phosphooctulonate_synthase 3-deoxy-8-phosphooctulonate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.55 2.5.1.55] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-deoxy-8-phosphooctulonate_synthase 3-deoxy-8-phosphooctulonate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.55 2.5.1.55] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkf OCA], [http://pdbe.org/2qkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qkf RCSB], [http://www.ebi.ac.uk/pdbsum/2qkf PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkf OCA], [http://pdbe.org/2qkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qkf RCSB], [http://www.ebi.ac.uk/pdbsum/2qkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qkf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qkf_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qkf_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 14:26, 5 September 2018
Crystal structure of 3-deoxy-d-manno-octulosonate 8-phosphate synthase (KDO8PS) from Neisseria meningitidisCrystal structure of 3-deoxy-d-manno-octulosonate 8-phosphate synthase (KDO8PS) from Neisseria meningitidis
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe analysis of the interaction of threose 4-phosphate and 2-deoxyerythrose 4-phosphate with 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS) reveals previously unrecognised mechanistic differences between the DAH7PS-catalysed reaction and that catalysed by the closely related enzyme, 3-deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8PS). Mechanistic divergence of two closely related aldol-like enzyme-catalysed reactions.,Ahn M, Pietersma AL, Schofield LR, Parker EJ Org Biomol Chem. 2005 Nov 21;3(22):4046-9. Epub 2005 Oct 6. PMID:16267580[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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